Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase

Scott Bailey; William K. Eliason; Thomas A. Steitz

doi:10.1126/science.1147353

Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase

Scott Bailey, William K. Eliason, Thomas A. Steitz

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153 Scopus citations

Abstract

The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at the eubacterial replication fork and synthesizes the Okazaki RNA primers. The crystal structures of hexameric DnaB and its complex with the helicase binding domain (HBD) of DnaG reveal that within the hexamer the two domains of DnaB pack with strikingly different symmetries to form a distinct two-layered ring structure. Each of three bound HBDs stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and thereby guide the DNA to a DnaG active site.

Original language	English (US)
Pages (from-to)	459-463
Number of pages	5
Journal	Science
Volume	318
Issue number	5849
DOIs	https://doi.org/10.1126/science.1147353
State	Published - Oct 19 2007
Externally published	Yes

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abstract = "The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at the eubacterial replication fork and synthesizes the Okazaki RNA primers. The crystal structures of hexameric DnaB and its complex with the helicase binding domain (HBD) of DnaG reveal that within the hexamer the two domains of DnaB pack with strikingly different symmetries to form a distinct two-layered ring structure. Each of three bound HBDs stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and thereby guide the DNA to a DnaG active site.",

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AU - Bailey, Scott

AU - Eliason, William K.

AU - Steitz, Thomas A.

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AB - The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at the eubacterial replication fork and synthesizes the Okazaki RNA primers. The crystal structures of hexameric DnaB and its complex with the helicase binding domain (HBD) of DnaG reveal that within the hexamer the two domains of DnaB pack with strikingly different symmetries to form a distinct two-layered ring structure. Each of three bound HBDs stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and thereby guide the DNA to a DnaG active site.

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Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase

Abstract

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